MALTOSE PHOSPHORYLASE
MALTOSE PHOSPHORYLASE structure
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Common Name | MALTOSE PHOSPHORYLASE | ||
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| CAS Number | 9030-19-7 | Molecular Weight | 807.879 | |
| Density | 1.4±0.1 g/cm3 | Boiling Point | 900.5±65.0 °C at 760 mmHg | |
| Molecular Formula | C43H53NO14 | Melting Point | N/A | |
| MSDS | USA | Flash Point | 498.4±34.3 °C | |
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Enzymatic synthesis of alpha-anomer-selective D-glucosides using maltose phosphorylase.
Biosci. Biotechnol. Biochem. 71 , 1598-1600, (2007) A maltose phosphorylase (EC 2.4.1.8; MPase) showed novel acceptor specificity and transferred the glucosyl moiety of maltose not only to sugars but also to various acceptors having alcoholic OH groups. Salicyl alcohol acted as acceptor for MPase from Enteroco... |
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Rational engineering of Lactobacillus acidophilus NCFM maltose phosphorylase into either trehalose or kojibiose dual specificity phosphorylase.
Protein Eng. Des. Sel. 23(10) , 781-7, (2010) Lactobacillus acidophilus NCFM maltose phosphorylase (LaMP) of the (alpha/alpha)(6)-barrel glycoside hydrolase family 65 (GH65) catalyses both phosphorolysis of maltose and formation of maltose by reverse phosphorolysis with beta-glucose 1-phosphate and gluco... |
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Development of a conductometric phosphate biosensor based on tri-layer maltose phosphorylase composite films.
Anal. Chim. Acta 615(1) , 73-9, (2008) A conductometric biosensor for phosphate detection was developed using maltose phosphorylase (MP) from recombinant Escherichia coli immobilized on a planar interdigitated electrode by cross-linking with saturated glutaraldehyde (GA) vapour in the presence of ... |
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Maltose phosphorylase from Lactobacillus brevis: purification, characterization, and application in a biosensor for ortho-phosphate.
Enzyme Microb. Technol. 21(6) , 413-20, (1997) With the goal to obtain maltose phosphorylase as a tool to determine ortho-phosphate, the enzyme from Lactobacillus brevis was purified to 98% by an expeditious FPLC-aided procedure which included anion exchange chromatography, gel filtration, and hydroxyapat... |
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Substrate-induced activation of maltose phosphorylase: interaction with the anomeric hydroxyl group of alpha-maltose and alpha-D-glucose controls the enzyme's glucosyltransferase activity.
Arch. Biochem. Biophys. 281(1) , 58-65, (1990) Maltose phosphorylase, long considered strictly specific for beta-D-glucopyranosyl phosphate (beta-D-glucose 1-P), was found to catalyze the reaction beta-D-glucosyl fluoride + alpha-D-glucose----alpha-maltose + HF, at a rapid rate, V = 11.2 +/- 1.2 mumol/(mi... |
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Maltose metabolism of Lactobacillus sanfranciscensis: cloning and heterologous expression of the key enzymes, maltose phosphorylase and phosphoglucomutase.
FEMS Microbiol. Lett. 169(1) , 81-6, (1998) The maltose degradation operon containing genes encoding maltose phosphorylase mapA and phosphoglucomutase pgmA from Lactobacillus sanfranciscensis DSM20451T were cloned and expressed in Escherichia coli. These genes represent the first genetic data available... |
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In-gel precipitation of enzymatically released phosphate.
Anal. Biochem. 334(2) , 312-7, (2004) The phosphate precipitation reaction using ammonium molybdate and triethylamine under low pH has been applied to gel-based assays for detecting phosphate-releasing enzymes. The sensitivity of the assay is 10 pmol Pi/mm2 of 1.5-mm-thick gel. The assay is appli... |
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Production and stabilization of pure maltose phosphorylase from Lactobacillus brevis for sensing inorganic phosphate.
Ann. N. Y. Acad. Sci. 799 , 701-6, (1996)
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Cloning of the maltose phosphorylase gene from Bacillus sp. strain RK-1 and efficient production of the cloned gene and the trehalose phosphorylase gene from Bacillus stearothermophilus SK-1 in Bacillus subtilis.
Biosci. Biotechnol. Biochem. 66(12) , 2594-9, (2002) The maltose phosphorylase (MPase) gene of Bacillus sp. strain RK-1 was cloned by PCR with oligonucleotide primers designed on the basis of a partial N-terminal amino acid sequence of the purified enzyme. The MPase gene consisted of 2,655 bp encoding a theoret... |
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Purification and characterization of maltose phosphorylase from Bacillus sp. RK-1.
Biosci. Biotechnol. Biochem. 65(12) , 2644-9, (2001) Bacillus sp. RK-1 was isolated as a bacterium that produced maltose phosphorylase (MPase) in the culture supernatant. Screening was done from among about 400 isolates that could grow at 55 degrees C in a medium containing maltose as the sole carbon source. Th... |